Investigation of the mechanism and steric course of the reaction catalyzed by 6-methylsalicylic acid synthase from Penicillium patulum using (R)-[1-13C;2-2H] and (S)-[1-13C; 2-2H]malonates

Biochemistry ◽  
1992 ◽  
Vol 31 (37) ◽  
pp. 9107-9116 ◽  
Author(s):  
Jonathan B. Spencer ◽  
Peter M. Jordan
Keyword(s):  
Methylsalicylic Acid Synthase ◽  
Penicillium Patulum

scholarly journals Purification and properties of 6-methylsalicylic acid synthase from Penicillium patulum

1992 ◽  
Vol 288 (3) ◽  
pp. 839-846 ◽  
Author(s):  
J B Spencer ◽  
P M Jordan
Keyword(s):  
Fatty Acid ◽  
Proteinase Inhibitors ◽  
Type I ◽  
Acetyl Coa ◽  
Purification Method ◽  
Methylsalicylic Acid Synthase ◽  
Acid Lactone ◽  
Penicillium Patulum ◽  
Triacetic Acid Lactone

6-Methylsalicylic acid synthase has been isolated in homogeneous form from Penicillium patulum grown in liquid culture from a spore inoculum. The enzyme is highly susceptible to proteolytic degradation in vivo and in vitro, but may be stabilized during purification by incorporating proteinase inhibitors in the buffers. The enzyme exists as a homotetramer of M(r) 750,000, with a subunit M(r) of 180,000. 6-Methylsalicyclic acid synthase also accepts acetoacetyl-CoA as an alternative starter molecule to acetyl-CoA. The enzyme also catalyses the formation of small amounts of triacetic acid lactone as an oligatory by-product of the reaction. In the absence of NADPH, triacetic acid lactone is the exclusive enzymic product, being formed at 10% of the rate of 6-methylsalicylic acid. The enzyme is inactivated by 1,3-dibromopropan-2-one, leading to the formation of cross-linked dimers similar to that observed with type I fatty acid synthases. Acetyl-CoA protects the enzyme against the inactivation and inhibits dimer formation. An adaptation of the purification method for 6-methylsalicylic acid synthase may be used for the isolation of fatty acid sythase from Penicillium patulum.

Proteolytic and Lipolytic Activities of some Toxigenic and Nontoxigenic Aspergilli and Penicillia

1980 ◽  
Vol 43 (5) ◽  
pp. 354-355 ◽  
Author(s):  
S. M. EL-GENDY ◽  
E. H. MARTH
Keyword(s):  
Proteolytic Activity ◽  
Aspergillus Flavus ◽  
Aspergillus Parasiticus ◽  
Lipolytic Activity ◽  
The Other ◽  
Aspergillus Ochraceus ◽  
Penicillium Roqueforti ◽  
Two Cultures ◽  
Penicillium Cyclopium ◽  
Penicillium Patulum

Eighteen strains of Aspergillus flavus or Aspergillus parasiticus, one of Aspergillus ochraceus and 12 strains or species of Penicillium, many of them isolated from cheese, were evaluated for their proteolytic and lipolytic activities. Strains of A. flavus exhibited considerable proteolytic and little lipolytic activity, whereas the reverse was true for strains of A. parasiticus. Of the Penicillium cultures tested, 10 exhibited considerable lipolytic activity, but only five had marked proteolytic activity. Two cultures, Penicillium patulum M59, and Penicillium cyclopium No. 8, were markedly lipolytic and proteolytic. Of the other cultures, greatest lipolytic activity was associated with Penicillium roqueforti 849, Penicillium puberulum No. 33, A. parasiticus NRRL 3145 and NRRL 465 and A. ochraceus NRRL 3174, whereas greatest proteolytic activity of all the cultures was associated with P. patulum M59, P. cyclopium No. 25 and A. flavus WB500, 4018, 4098 and NRRL 5565.

Tolerance and Specificity of Recombinant 6-Methylsalicylic Acid Synthase

1999 ◽  
Vol 1 (2) ◽  
pp. 180-187 ◽  
Author(s):  
Maia T. Richardson ◽  
Nicola L. Pohl ◽  
James T. Kealey ◽  
Chaitan Khosla
Keyword(s):  
Methylsalicylic Acid Synthase

Structural Similarities between 6-Methylsalicylic Acid Synthase fromPenicillium patulumand Vertebrate Type I Fatty Acid Synthase:  Evidence from Thiol Modification Studies†

Biochemistry ◽  
1996 ◽  
Vol 35 (38) ◽  
pp. 12267-12274 ◽  
Author(s):  
Christopher J. Child ◽  
Jonathan B. Spencer ◽  
Pamela Bhogal ◽  
Peter M. Shoolingin-Jordan
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Type I ◽  
Methylsalicylic Acid Synthase

Isolation and sequence analysis of the fatty acid synthetase FAS2 gene from Penicillium patulum

1988 ◽  
Vol 177 (1) ◽  
pp. 69-79 ◽  
Author(s):  
Peter WIESNER ◽  
Joachim BECK ◽  
Karl-Friedrich BECK ◽  
Sabine RIPKA ◽  
Gerhard MULLER ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Sequence Analysis ◽  
Fatty Acid Synthetase ◽  
Penicillium Patulum
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